DHSD_CAEBR
ID DHSD_CAEBR Reviewed; 145 AA.
AC A8WT26;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Putative succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE AltName: Full=Succinate dehydrogenase complex subunit D {ECO:0000250|UniProtKB:Q5ZIS0};
DE Flags: Precursor;
GN Name=sdhd-1 {ECO:0000312|EMBL:CAP23637.1}; ORFNames=CBG02978;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP23637.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP23637.1};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH)
CC that is involved in complex II of the mitochondrial electron transport
CC chain and is responsible for transferring electrons from succinate to
CC ubiquinone (coenzyme Q). {ECO:0000250|UniProtKB:Q5ZIS0}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000305}.
CC -!- SUBUNIT: Forms part of complex II containing four subunits: a
CC flavoprotein (FP), an iron-sulfur protein (IP) and a cytochrome b
CC composed of a large and a small subunit.
CC {ECO:0000250|UniProtKB:Q5ZIS0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q5ZIS0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5ZIS0}.
CC -!- SIMILARITY: Belongs to the CybS family. {ECO:0000255}.
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DR EMBL; HE601438; CAP23637.1; -; Genomic_DNA.
DR RefSeq; XP_002631189.1; XM_002631143.1.
DR AlphaFoldDB; A8WT26; -.
DR SMR; A8WT26; -.
DR STRING; 6238.CBG02978; -.
DR EnsemblMetazoa; CBG02978.1; CBG02978.1; WBGene00025932.
DR GeneID; 8572703; -.
DR KEGG; cbr:CBG_02978; -.
DR CTD; 8572703; -.
DR WormBase; CBG02978; CBP00616; WBGene00025932; Cbr-sdhd-1.
DR eggNOG; KOG4097; Eukaryota.
DR HOGENOM; CLU_096618_1_1_1; -.
DR InParanoid; A8WT26; -.
DR OMA; KLERLWA; -.
DR OrthoDB; 1511215at2759; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd03496; SQR_TypeC_CybS; 1.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR007992; CybS.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR PANTHER; PTHR13337; PTHR13337; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..145
FT /note="Putative succinate dehydrogenase [ubiquinone]
FT cytochrome b small subunit, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000367045"
FT TOPO_DOM 1..52
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..75
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..108
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..145
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 84
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with large subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q5ZIS0"
FT BINDING 96
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with IP"
FT /evidence="ECO:0000250|UniProtKB:Q5ZIS0"
SQ SEQUENCE 145 AA; 15765 MW; 5CE32B124BAD3A8B CRC64;
MAASLRHMAH FQKALLVAKT APRLSTIVRA TSTLNDGASK VPDHSMHFKL ERLWAVGMLP
ILPASYFIHG PVMDAVLTVA LTLHIHWGIH GVVYDYARPY VIGEAAAKAA HIGVYLITGL
LLAGLLHFNT NDVGITKAFE LVFSL
